Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.
Identifieur interne : 000E97 ( Main/Exploration ); précédent : 000E96; suivant : 000E98Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.
Auteurs : W J Bao [États-Unis] ; V. RenganathanSource :
- FEBS letters [ 0014-5793 ] ; 1991.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Cellobiose, Flavines, Iodures.
- enzymologie : Basidiomycota.
- métabolisme : Carbohydrate dehydrogenases.
- Catalyse, Myeloperoxidase, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cellobiose, Flavins, Iodides.
- chemical , metabolism : Carbohydrate Dehydrogenases.
- enzymology : Basidiomycota.
- Catalysis, Oxidation-Reduction, Peroxidase.
Abstract
Cellobiose:quinone oxidoreductase (CBQase) in the presence of cellobiose inhibits peroxidase-catalyzed oxidation of iodide to triiodide (I3). This inhibition is due to the two-electron reduction of I3- by CBQase. The apparent Km of I3- for this reaction is 120 microM and the specific activity is 57 mumol.min-1.mg-1. A proposed mechanism for I3- reduction by CBQase involves initial reduction of the flavin moiety by cellobiose to produce a dihydroflavin. This is followed by the substitution of one of the iodine atoms of I3- at the C(4a)-position of dihydroflavin to generate C(4a)-iododihydroflavin and two iodide ions. The C(4a)-iododihydroflavin eliminates HI to regenerate the oxidized CBQase.
DOI: 10.1016/0014-5793(91)80242-u
PubMed: 1847342
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Bao, W J" sort="Bao, W J" uniqKey="Bao W" first="W J" last="Bao">W J Bao</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton, OR 97006-1999.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Oregon</region>
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<wicri:cityArea>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton</wicri:cityArea>
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<author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.</title>
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<affiliation wicri:level="2"><nlm:affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton, OR 97006-1999.</nlm:affiliation>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term>
<term>Carbohydrate Dehydrogenases (metabolism)</term>
<term>Catalysis (MeSH)</term>
<term>Cellobiose (chemistry)</term>
<term>Flavins (chemistry)</term>
<term>Iodides (chemistry)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidase (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term>
<term>Carbohydrate dehydrogenases (métabolisme)</term>
<term>Catalyse (MeSH)</term>
<term>Cellobiose (composition chimique)</term>
<term>Flavines (composition chimique)</term>
<term>Iodures (composition chimique)</term>
<term>Myeloperoxidase (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellobiose</term>
<term>Flavins</term>
<term>Iodides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellobiose</term>
<term>Flavines</term>
<term>Iodures</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carbohydrate dehydrogenases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalysis</term>
<term>Oxidation-Reduction</term>
<term>Peroxidase</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term>
<term>Myeloperoxidase</term>
<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">Cellobiose:quinone oxidoreductase (CBQase) in the presence of cellobiose inhibits peroxidase-catalyzed oxidation of iodide to triiodide (I3). This inhibition is due to the two-electron reduction of I3- by CBQase. The apparent Km of I3- for this reaction is 120 microM and the specific activity is 57 mumol.min-1.mg-1. A proposed mechanism for I3- reduction by CBQase involves initial reduction of the flavin moiety by cellobiose to produce a dihydroflavin. This is followed by the substitution of one of the iodine atoms of I3- at the C(4a)-position of dihydroflavin to generate C(4a)-iododihydroflavin and two iodide ions. The C(4a)-iododihydroflavin eliminates HI to regenerate the oxidized CBQase.</div>
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<Month>03</Month>
<Day>27</Day>
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<DateRevised><Year>2019</Year>
<Month>06</Month>
<Day>20</Day>
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<Day>11</Day>
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<Title>FEBS letters</Title>
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<ArticleTitle>Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract><AbstractText>Cellobiose:quinone oxidoreductase (CBQase) in the presence of cellobiose inhibits peroxidase-catalyzed oxidation of iodide to triiodide (I3). This inhibition is due to the two-electron reduction of I3- by CBQase. The apparent Km of I3- for this reaction is 120 microM and the specific activity is 57 mumol.min-1.mg-1. A proposed mechanism for I3- reduction by CBQase involves initial reduction of the flavin moiety by cellobiose to produce a dihydroflavin. This is followed by the substitution of one of the iodine atoms of I3- at the C(4a)-position of dihydroflavin to generate C(4a)-iododihydroflavin and two iodide ions. The C(4a)-iododihydroflavin eliminates HI to regenerate the oxidized CBQase.</AbstractText>
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<Chemical><RegistryNumber>EC 1.1.-</RegistryNumber>
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<Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber>
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